Immobilisation of glycosidases from commercial preparation on magnetic beads. Part 2: Aroma enhancement in wine using immobilised glycosidases

Abstract

Most of the terpenes in wines are conjugated to various sugars, representing a significant reservoir of aromatic precursors. To promote the release of these terpenes, certain enzymes, such as β-glucosidase, α-arabinosidase and α-rhamnosidase, are necessary. A simple and cost-effective procedure for the immobilisation of multiple glycosidase activities (β-D-glucopyranosidase, α-L-arabinofuranosidase, α-L-rhamnopyranosidase and β-D-xylopyranosidase) from commercial Aspergillus niger preparation onto magnetic beads as carriers was developed as reported in Part 1 (Ferner et al. 2016). The aim of this work was to analyse a possible application of this immobilised biocatalyst due to its well-known advantages over soluble enzyme preparations – that is, control of the reaction process and preparation of enzyme-free products. Volatile compounds were analysed by gas chromatography (mass spectrometric detection). After the treatment of the model wine with different glycosides and white wine with immobilised glycosidases, the amount of free terpenes was significantly increased with respect to that of the control wine. The results of this study are of considerable interest for possible future applications of immobilised enzymes in the wine-making industry.